reaction from bicyclic C-8 cation (chair-boat form) via protosteryl cation (chair-boat-chair form) to parkeol, proposed reaction scheme of cyclization, overview
reaction from bicyclic C-8 cation (chair-boat form) via protosteryl cation (chair-boat-chair form) to parkeol, proposed reaction scheme of cyclization, overview
molecular evolutionary analysis. Phylogenetic, network and functional analyses of OsOSC7 variants in Oryza sativa subsp. japonica and in Oryza wild-type species, overview
molecular evolutionary analysis. Phylogenetic, network and functional analyses of OsOSC7 variants in Oryza sativa subsp. japonica and in Oryza wild-type species, overview
identification of three key amino acid residues amongst 46 polymorphic sites that determine functional conversion between tetracyclic parkeol synthase (OsPS) and pentacyclic orysatinol synthase (OsOS), specifically, the chair-semi(chair)-chair and chair-boat-chair interconversions. Mechanism for the function conversion between OsPS and OsOS. The different orientation of a fourth amino acid residue Y257 is important for functional conversion. Three-dimensional modeling of the enzyme proteins generated by using Homo sapiens LAS structure (PDB ID 1W6K) as a template. Ligand docking
identification of three key amino acid residues amongst 46 polymorphic sites that determine functional conversion between tetracyclic parkeol synthase (OsPS) and pentacyclic orysatinol synthase (OsOS), specifically, the chair-semi(chair)-chair and chair-boat-chair interconversions. Mechanism for the function conversion between OsPS and OsOS. The different orientation of a fourth amino acid residue Y257 is important for functional conversion. Three-dimensional modeling of the enzyme proteins generated by using Homo sapiens LAS structure (PDB ID 1W6K) as a template. Ligand docking
mutant produces lanosterol, parkeol, 9beta-lanosta-7,24-dien-3 beta-ol, protosta-13(17),24-dien-3beta-ol and protosta-16,24-dien-3beta-ol in the ratio of 63:31.5:3.5:1:1 without compounds achilleol A and (13alphaH)-isomalabarica-14(26),17E,21-trien-3 beta-ol
gene OsOP, from leaf sheath material, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression in Pichia pastoris strain X33 under the control of the methanol-inducible promoter AOX1
Oxidosqualene Cyclase Residues that Promote Formation of Cycloartenol, Lanosterol, and Parkeol We are grateful to Bridget M. Joubert for advice regarding mutagenesis. We thank Elizabeth A. Hart for an authentic parkeol standard, and for chromatographic and spectroscopic information. This research was funded by the National Institutes of Health (grant no. AI 41598) and the Robert A. Welch Foundation (grant no. C-1323). M.M.M. was an American Society of Pharmacognosy Undergraduate Fellow. M.J.R.S. was a Robert A. Welch Fellow and was supported by an NIH Biotechnology Training Grant (grant no. T32 GM08362).
Histidine residue at position 234 of oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae simultaneously influences cyclization, rearrangement, and deprotonation reactions
Directed evolution to investigate steric control of enzymatic oxidosqualene cyclization. An isoleucine-to-valine mutation in cycloartenol synthase allows lanosterol and parkeol biosynthesis
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